Regulation of nitrate reductase levels in the cyanobacteria Anacystis nidulans, Anabaena sp. strain 7119, and Nostoc sp. strain 6719.
The effect of the nitrogen source on the cellular activity of ferredoxin-nitrate reductase in different cyanobacteria was examined. In the unicellular species Anacystis nidulans, nitrate reductase was repressed in the presence of ammonium but de novo enzyme synthesis took place in media containing either nitrate or not nitrogen source, indicating that nitrate was not required as an obligate inducer. Nitrate reductase in A. nidulans was freed from ammonium repression by L-methionine-D,L-sulfoximine, an irreversible inhibitor of glutamine synthetase. Ammonium-promoted repression appears therefore to be indirect; ammonium has to be metabolized through glutamine synthetase to be effective in the repression of nitrate reductase. Unlike the situation in A. nidulans, nitrate appeared to play an active role in nitrate reductase synthesis in the filamentous nitrogen-fixing strains Anabaena sp. strain 7119 and Nostoc sp. strain 6719, with ammonium acting as an antagonist with regard to nitrate.
D000645:Ammonium Sulfate / Q000494:pharmacology; D003470:Culture Media; D000458:Cyanobacteria / Q000201:enzymology*; D004794:Enzyme Repression; D008717:Methionine Sulfoximine / Q000494:pharmacology; D009565:Nitrate Reductases / Q000378:metabolism*; D009566:Nitrates / Q000494:pharmacology
D003470:Culture Media; D009566:Nitrates; D008717:Methionine Sulfoximine; D009565:Nitrate Reductases; D000645:Ammonium Sulfate